Nipah virus (NiV) infection remains a significant public health threat due to its high mortality rate. currently there are No approved antiviral therapeutics exist, necessitating the development of selective and effective antiviral agents. The viral attachment glycoprotein (G) is a well-established molecular target, as receptorbinding interactions are critical for host cell entry and disease progression. In the present study, a library of 60 heterocyclic derivatives was designed and computationally evaluated as potential Nipah virus glycoprotein inhibitors, comprising 30 pyrazole-based (PP) and 30 triazole-based (T series) compounds. Molecular docking studies against the Nipah virus glycoprotein (PDB ID: 2VSM) revealed favorable binding energies, ranging from -7.8 to -9.5 kcal/mol for the pyrazole series and -6.9 to -8.8 kcal/mol for the triazole series. Compounds exhibited strong hydrogen bonding and hydrophobic interactions with crucial active-site residues, includingGLN559, GLN530, ALA532, and GLY506. Compounds with highest binding energy were synthesized (PP3, PP9, PP17, PP18, PP20, T2, T4, T5, T9, T18) and characterization using IR, ¹H-NMR and Mass spectrometry, for the structural conformation. The synthesized compounds were screened for in-vitro antiviral potential using the CPE inhibition assay in Vero E6 cell-line. Compound PP3 and T18 emerged as the most potent leads, with EC5 0 values of 19.83 mm and 21.18 mm respectively when compared with Ribavirin (EC 5 0 = 12.48mm) as a standard drug. Overall, these findings suggest that the designed pyrazole and triazole derivatives as promising Nipah virus glycoprotein inhibitors, providing a strong foundation for further lead optimization and preclinical evaluation.